Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | dependent on | Pseudomonas syringae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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additional information | Pseudomonas syringae | the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed | ? | - |
? | |
additional information | Pseudomonas syringae B301D | the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed | ? | - |
? |
Organism | UniProt | Comment | Textmining |
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Pseudomonas syringae | - |
- |
- |
Pseudomonas syringae B301D | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed | Pseudomonas syringae | ? | - |
? | |
additional information | non-native substrates undergo hydroxylation as well as chlorination. The cis-chloroferryl complex in enzyme SyrB2 reacts more rapidly with SyrB1 presenting L-aminobutyric acid or L-norvaline than with L-threonine. Selectivity for chlorination is also strongly modulated: L-threonine is almost exclusively chlorinated, L-aminobutyric acid is chlorinated and hydroxylated at C4 to similar extents, and L-norvaline is predominately hydroxylated at the C5 position. The differential reactivity observed for the different substrates might arise primarily from substrate-protein interactions that impact the partition between the axial and equatorial coordination isomers of the ferryl complex rather than from substrate positioning per se | Pseudomonas syringae | ? | - |
? | |
additional information | the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed | Pseudomonas syringae B301D | ? | - |
? | |
additional information | non-native substrates undergo hydroxylation as well as chlorination. The cis-chloroferryl complex in enzyme SyrB2 reacts more rapidly with SyrB1 presenting L-aminobutyric acid or L-norvaline than with L-threonine. Selectivity for chlorination is also strongly modulated: L-threonine is almost exclusively chlorinated, L-aminobutyric acid is chlorinated and hydroxylated at C4 to similar extents, and L-norvaline is predominately hydroxylated at the C5 position. The differential reactivity observed for the different substrates might arise primarily from substrate-protein interactions that impact the partition between the axial and equatorial coordination isomers of the ferryl complex rather than from substrate positioning per se | Pseudomonas syringae B301D | ? | - |
? |
Synonyms | Comment | Organism |
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aliphatic halogenase | - |
Pseudomonas syringae |
SyrB2 | - |
Pseudomonas syringae |
General Information | Comment | Organism |
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evolution | the enzyme SyrB2 from Pseudomonas syringae B301D is the founding member of the Fe/2OG aliphatic halogenases. In SyrB2, the sequence position that normally provides the carboxylate of the canonical facial triad of protein ligands is occupied by an alanine (Ala118), and the co-substrate, chloride (Cl?), occupies the vacated site in the iron coordination sphere.32 Fe/2OG halogenases mechanistically parallel the hydroxylases in that both employ ferryl intermediates as the H-abstracting species | Pseudomonas syringae |
additional information | other factors might be involved in directing the halogenation outcome and the likelihood that proper substrate positioning is also essential to avoidance of hydroxylation in the other types of Fe/2OG-oxygenase reactivity, direct probing the positions of the various target C-H bonds relative to the iron center, coupling of NO, overview | Pseudomonas syringae |